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B6db families: 2.6.1.13.a

2.6.1.13 a
Activity 2.6.1.13
Description Ornithine--oxo-acid aminotransferase (family a)
Notes The enzyme from Penicillium chrysogenum employs as substrates both L-ornithine (yielding L-glutamate 5-semialdehyde) and L-lysine (yielding L-aminoadipate semialdehyde). The latter reaction is important for the biosynthesis of penicillin. Given its structural similarity to classic ornithine aminotransferases, and its preference for alpha-ketoglutarate as an amino acceptor, we have included the enzyme from Penicillium in the 2.6.1.13 family, rather than among L-lysine aminotransferases (EC 2.6.1.36) or omega-amino acid--pyruvate aminotransferases (EC 2.6.1.18).
PDB 1GBN;2OAT;1Z7D;4ZWM;
PLP Fold Type I
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type I

Reference sequence OAT_HUMAN
Domain interval 61-384
Catalytic site 292 K
 
References
 Astegno A, Maresi E, Bertoldi M, La Verde V, Paiardini A, Dominici P (2017) Unique substrate specificity of ornithine aminotransferase from Toxoplasma gondii Biochem J 474 939-955.

 Hampel A, Huber C, Geffers R, Spona-Friedl M, Eisenreich W, Bange FC (2015) Mycobacterium tuberculosis is a natural ornithine aminotransferase (rocD) mutant and depends on Rv2323c for growth on arginine PLoS One 10 e0136914..

 Funck D, Stadelhofer B, Koch W. (2008) Ornithine-[delta]-aminotransferase is essential for arginine catabolism but not for proline biosynthesis BMC Plant Biol 8 40.

 Valmaseda, E.M.; Campoy, S.; Naranjo, L.; Casqueiro, J.; Martin, J.F. (2005) Lysine is catabolized to 2-aminoadipic acid in Penicillium chrysogenum by an omega-aminotransferase and to saccharopine by a lysine 2-ketoglutarate reductase. Characterization of the omega-aminotransferase Mol Genet Genomics 274 272-82.

 Gafan, C.; Wilson, J.; Berger, L.C.; Berger, B.J. (2001) Characterization of the ornithine aminotransferase from Plasmodium falciparum. Mol Biochem Parasitol 118 1-10.

 Jhee, K. H.; Yoshimura, T.; Esaki, N.; Yonaha, K.; Soda, K. (1995) Thermostable ornithine aminotransferase from Bacillus sp. YM-2: purification and characterization J Biochem (Tokyo) 118 101-8.

 Takechi M, Kanda M, Hori K, Kurotsu T, Saito Y. (1994) Purification and properties of L-ornithine delta-aminotransferase from gramicidin S-producing Bacillus brevis J Biochem 116 955-9.

 Delauney, A.J.; Hu, C.A.; Kishor, P.B.; Verma, D.P. (1993) Cloning of ornithine delta-aminotransferase cDNA from Vigna aconitifolia by trans-complementation in Escherichia coli and regulation of proline biosynthesis J Biol Chem 268 18673-8.

 Simmaco, M.; John, R. A.; Barra, D.; Bossa, F. (1986) The primary structure of ornithine aminotransferase. Identification of active-site sequence and site of post-translational proteolysis FEBS Lett 199 39-42.

Articles on 2.6.1.13.a
last changed 2018/01/23 11:05

B6db families